1prx
From Proteopedia
HORF6 A NOVEL HUMAN PEROXIDASE ENZYME
Structural highlights
FunctionPRDX6_HUMAN Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.,Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE Nat Struct Biol. 1998 May;5(5):400-6. PMID:9587003[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
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Categories: Homo sapiens | Large Structures | Choi H-J | Kang SW | Rhee SG | Ryu S-E | Yang C-H
